Structure and function of yeast Atg20, a sorting nexin that facilitates autophagy induction

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Abstract

The Atg20 and Snx4/Atg24 proteins have been identified in a screen for mutants defective in a type of selective macroautophagy/autophagy. Both proteins are connected to the Atg1 kinase complex, which is involved in autophagy initiation, and bind phosphatidylinositol-3-phosphate. Atg20 and Snx4 contain putative BAR domains, suggesting a possible role in membrane deformation, but they have been relatively uncharacterized. Here we demonstrate that, in addition to its function in selective autophagy, Atg20 plays a critical role in the efficient induction of nonselective autophagy. Atg20 is a dynamic posttranslationally modified protein that engages both structurally stable (PX and BAR) and intrinsically disordered domains for its function. In addition to its PX and BAR domains, Atg20 uses a third membrane-binding module, a membrane-inducible amphipathic helix present in a previously undescribed location in Atg20 within the putative BAR domain. Taken together, these findings yield insights into the molecular mechanism of the autophagy machinery.

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Popelka, H., Damasio, A., Hinshaw, J. E., Klionsky, D. J., & Ragusa, M. J. (2017). Structure and function of yeast Atg20, a sorting nexin that facilitates autophagy induction. Proceedings of the National Academy of Sciences of the United States of America, 114(47), E10112–E10121. https://doi.org/10.1073/pnas.1708367114

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